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. Author manuscript; available in PMC: 2011 Mar 14.
Published in final edited form as: Structure. 2010 Mar 14;18(4):436–448. doi: 10.1016/j.str.2010.01.013

Figure 3. Structures of the Aer2 HAMP Domains.

Figure 3

Side and top views (90° rotation) of individual Aer2 HAMP domains with buried side chains (Carbon: yellow to red, Nitrogen: blue, Sulfur: green). HAMP1 and HAMP3 sidechains are in-register and HAMP2 sidechains are offset. HAMP2 has an unusual trapezoidal shape (as viewed from the side) and rhombic arrangement of helices in cross section. The position of the connector and hydrophobic residue 2 (HR2) correlates with changes in helical register, helix crossing angles, and helical rotation. I88 (HR2, HAMP2) inserts between AS1 and AS2, and V33 (HR2, HAMP1) and M134 (HR2, HAMP3) pack against the periphery of AS1 and AS2.